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PCAentropy_SquE.pdf (1.47 MB)
Long-Range Entropic Effects on Protein Intrinsically Disordered Regions
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Entropy calculations represent one of the most challenging steps in obtaining the binding free energy in proteins and their complexes, which is a grand challenge in computational biology. In this paper we define the workframe of a novel method to calculate structural entropy for protein molecular simulation : SQuE ( Strucutral Quantifier of Entropy). Using a first degree approximation for the probability distribution, we were able to calculate the entropic effects that emerges from a intrinsically disordered (ID) region in UDP-glucose 6-dehydrogenase (UGDH) protein structure. We were able to quantify the configurational entropy difference in the structured core caused by the truncation of the C-terminal ID-tail, and evaluate the protein conformational changes in the structured domain.